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Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]

 TGFB1_HUMAN             Reviewed;         390 AA.
P01137; A8K792; Q9UCG4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
17-JUN-2020, entry version 254.
RecName: Full=Transforming growth factor beta-1 proprotein;
Contains:
RecName: Full=Latency-associated peptide {ECO:0000305|PubMed:2982829, ECO:0000305|PubMed:3162913, ECO:0000305|PubMed:7737999, ECO:0000305|PubMed:8471846};
Short=LAP;
Contains:
RecName: Full=Transforming growth factor beta-1 {ECO:0000305|PubMed:2982829, ECO:0000305|PubMed:3162913, ECO:0000305|PubMed:7737999, ECO:0000305|PubMed:8471846};
Short=TGF-beta-1;
Flags: Precursor;
Name=TGFB1 {ECO:0000312|HGNC:HGNC:11766}; Synonyms=TGFB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3470709; DOI=10.1093/nar/15.7.3188;
Derynck R., Rhee L., Chen E.Y., van Tilburg A.;
"Intron-exon structure of the human transforming growth factor-beta
precursor gene.";
Nucleic Acids Res. 15:3188-3189(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PRO-10 AND PRO-25.
PubMed=3861940; DOI=10.1038/316701a0;
Derynck R., Jarrett J.A., Chen E.Y., Eaton D.H., Bell J.R., Assoian R.K.,
Roberts A.B., Sporn M.B., Goeddel D.V.;
"Human transforming growth factor-beta complementary DNA sequence and
expression in normal and transformed cells.";
Nature 316:701-705(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Duodenum, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 279-390.
TISSUE=Carcinoma;
Urushizaki Y., Niitsu Y., Terui T., Koshida Y., Mahara K., Kohgo Y.,
Urushizaki I., Takahashi Y., Ito H.;
"Cloning and expression of the gene for human transforming growth factor-
beta in Escherichia coli.";
Tumor Res. 22:41-55(1987).
[8]
PROTEIN SEQUENCE OF 279-329.
TISSUE=Urinary bladder carcinoma;
PubMed=8471846; DOI=10.1006/prep.1993.1019;
Bourdrel L., Lin C.-H., Lauren S.L., Elmore R.H., Sugarman B.J., Hu S.,
Westcott K.R.;
"Recombinant human transforming growth factor-beta 1: expression by Chinese
hamster ovary cells, isolation, and characterization.";
Protein Expr. Purif. 4:130-140(1993).
[9]
PROTEIN SEQUENCE OF 279-301.
PubMed=2982829;
Massague J., Like B.;
"Cellular receptors for type beta transforming growth factor. Ligand
binding and affinity labeling in human and rodent cell lines.";
J. Biol. Chem. 260:2636-2645(1985).
[10]
PROTEIN SEQUENCE OF 30-42 AND 279-290, AND GLYCOSYLATION.
PubMed=3162913;
Miyazono K., Hellman U., Wernstedt C., Heldin C.H.;
"Latent high molecular weight complex of transforming growth factor beta 1.
Purification from human platelets and structural characterization.";
J. Biol. Chem. 263:6407-6415(1988).
[11]
PROTEIN SEQUENCE OF 279-283, AND PROTEOLYTIC CLEAVAGE.
PubMed=7737999; DOI=10.1074/jbc.270.18.10618;
Dubois C.M., Laprise M.H., Blanchette F., Gentry L.E., Leduc R.;
"Processing of transforming growth factor beta 1 precursor by human furin
convertase.";
J. Biol. Chem. 270:10618-10624(1995).
[12]
GLYCOSYLATION.
PubMed=2493139; DOI=10.1038/338158a0;
Miyazono K., Heldin C.H.;
"Role for carbohydrate structures in TGF-beta 1 latency.";
Nature 338:158-160(1989).
[13]
INTERACTION WITH LTBP1.
PubMed=2022183; DOI=10.1002/j.1460-2075.1991.tb08049.x;
Miyazono K., Olofsson A., Colosetti P., Heldin C.H.;
"A role of the latent TGF-beta 1-binding protein in the assembly and
secretion of TGF-beta 1.";
EMBO J. 10:1091-1101(1991).
[14]
INTERACTION WITH LTBP1, AND MUTAGENESIS OF CYS-33.
PubMed=8617200; DOI=10.1002/j.1460-2075.1996.tb00355.x;
Saharinen J., Taipale J., Keski-Oja J.;
"Association of the small latent transforming growth factor-beta with an
eight cysteine repeat of its binding protein LTBP-1.";
EMBO J. 15:245-253(1996).
[15]
INTERACTION WITH LTBP1.
PubMed=8939931; DOI=10.1074/jbc.271.47.29891;
Gleizes P.E., Beavis R.C., Mazzieri R., Shen B., Rifkin D.B.;
"Identification and characterization of an eight-cysteine repeat of the
latent transforming growth factor-beta binding protein-1 that mediates
bonding to the latent transforming growth factor-beta1.";
J. Biol. Chem. 271:29891-29896(1996).
[16]
REVIEW.
PubMed=9150447; DOI=10.1038/ki.1997.188;
Munger J.S., Harpel J.G., Gleizes P.E., Mazzieri R., Nunes I., Rifkin D.B.;
"Latent transforming growth factor-beta: structural features and mechanisms
of activation.";
Kidney Int. 51:1376-1382(1997).
[17]
INTERACTION WITH DPT.
PubMed=9895299; DOI=10.1042/bj3370537;
Okamoto O., Fujiwara S., Abe M., Sato Y.;
"Dermatopontin interacts with transforming growth factor beta and enhances
its biological activity.";
Biochem. J. 337:537-541(1999).
[18]
TISSUE SPECIFICITY.
PubMed=11746498; DOI=10.1002/jcb.1249;
Shur I., Lokiec F., Bleiberg I., Benayahu D.;
"Differential gene expression of cultured human osteoblasts.";
J. Cell. Biochem. 83:547-553(2001).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[20]
INTERACTION WITH CD109.
PubMed=16754747; DOI=10.1096/fj.05-5229fje;
Finnson K.W., Tam B.Y.Y., Liu K., Marcoux A., Lepage P., Roy S.,
Bizet A.A., Philip A.;
"Identification of CD109 as part of the TGF-beta receptor system in human
keratinocytes.";
FASEB J. 20:1525-1527(2006).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[22]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH ASPN.
PubMed=17827158; DOI=10.1074/jbc.m700522200;
Nakajima M., Kizawa H., Saitoh M., Kou I., Miyazono K., Ikegawa S.;
"Mechanisms for asporin function and regulation in articular cartilage.";
J. Biol. Chem. 282:32185-32192(2007).
[23]
FUNCTION, AND INTERACTION WITH LRRC32.
PubMed=19750484; DOI=10.1002/eji.200939684;
Stockis J., Colau D., Coulie P.G., Lucas S.;
"Membrane protein GARP is a receptor for latent TGF-beta on the surface of
activated human Treg.";
Eur. J. Immunol. 39:3315-3322(2009).
[24]
FUNCTION, INTERACTION WITH LRRC32, AND MUTAGENESIS OF CYS-33.
PubMed=22278742; DOI=10.1091/mbc.e11-12-1018;
Wang R., Zhu J., Dong X., Shi M., Lu C., Springer T.A.;
"GARP regulates the bioavailability and activation of TGFbeta.";
Mol. Biol. Cell 23:1129-1139(2012).
[25]
FUNCTION, AND INTERACTION WITH LRRC32.
PubMed=19651619; DOI=10.1073/pnas.0901944106;
Tran D.Q., Andersson J., Wang R., Ramsey H., Unutmaz D., Shevach E.M.;
"GARP (LRRC32) is essential for the surface expression of latent TGF-beta
on platelets and activated FOXP3+ regulatory T cells.";
Proc. Natl. Acad. Sci. U.S.A. 106:13445-13450(2009).
[26]
INTERACTION WITH HSP90AB1.
PubMed=20599762; DOI=10.1016/j.bbrc.2010.06.112;
Suzuki S., Kulkarni A.B.;
"Extracellular heat shock protein HSP90beta secreted by MG63 osteosarcoma
cells inhibits activation of latent TGF-beta1.";
Biochem. Biophys. Res. Commun. 398:525-531(2010).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
FUNCTION.
PubMed=25310401; DOI=10.1371/journal.pone.0108528;
Chen Q., Lee C.E., Denard B., Ye J.;
"Sustained induction of collagen synthesis by TGF-beta requires regulated
intramembrane proteolysis of CREB3L1.";
PLoS ONE 9:E108528-E108528(2014).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[30]
FUNCTION.
PubMed=25893292; DOI=10.1038/onc.2015.100;
Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H., Lee J.H.;
"Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-
to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I
receptor internalization.";
Oncogene 35:389-401(2016).
[31]
REVIEW.
PubMed=27252363; DOI=10.1101/cshperspect.a021907;
Robertson I.B., Rifkin D.B.;
"Regulation of the bioavailability of TGF-beta and TGF-beta-related
proteins.";
Cold Spring Harb. Perspect. Biol. 8:0-0(2016).
[32]
FUNCTION, AND INTERACTION WITH NRROS.
PubMed=29909984; DOI=10.1016/j.cell.2018.05.027;
Qin Y., Garrison B.S., Ma W., Wang R., Jiang A., Li J., Mistry M.,
Bronson R.T., Santoro D., Franco C., Robinton D.A., Stevens B., Rossi D.J.,
Lu C., Springer T.A.;
"A milieu molecule for TGF-beta required for microglia function in the
nervous system.";
Cell 174:156-171(2018).
[33]
FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN IBDIMDE, VARIANTS IBDIMDE
CYS-45; CYS-110 AND ARG-387, AND CHARACTERIZATION OF VARIANTS IBDIMDE
CYS-45; CYS-110 AND ARG-387.
PubMed=29483653; DOI=10.1038/s41588-018-0063-6;
Kotlarz D., Marquardt B., Baroey T., Lee W.S., Konnikova L., Hollizeck S.,
Magg T., Lehle A.S., Walz C., Borggraefe I., Hauck F., Bufler P., Conca R.,
Wall S.M., Schumacher E.M., Misceo D., Frengen E., Bentsen B.S.,
Uhlig H.H., Hopfner K.P., Muise A.M., Snapper S.B., Stroemme P., Klein C.;
"Human TGF-beta1 deficiency causes severe inflammatory bowel disease and
encephalopathy.";
Nat. Genet. 50:344-348(2018).
[34]
FUNCTION.
PubMed=30696809; DOI=10.1038/s41419-019-1308-8;
Kim J.H., Ham S., Lee Y., Suh G.Y., Lee Y.S.;
"TTC3 contributes to TGF-beta1-induced epithelial-mesenchymal transition
and myofibroblast differentiation, potentially through SMURF2
ubiquitylation and degradation.";
Cell Death Dis. 10:92-92(2019).
[35]
STRUCTURE BY NMR OF 279-390.
PubMed=8424942; DOI=10.1021/bi00055a021;
Archer S.J., Bax A., Roberts A.B., Sporn M.B., Ogawa Y., Piez K.A.,
Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J.,
Torchia D.A.;
"Transforming growth factor beta 1: NMR signal assignments of the
recombinant protein expressed and isotopically enriched using Chinese
hamster ovary cells.";
Biochemistry 32:1152-1163(1993).
[36]
STRUCTURE BY NMR OF 279-390.
PubMed=8424943; DOI=10.1021/bi00055a022;
Archer S.J., Bax A., Roberts A.B., Sporn M.B., Ogawa Y., Piez K.A.,
Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J.,
Torchia D.A.;
"Transforming growth factor beta 1: secondary structure as determined by
heteronuclear magnetic resonance spectroscopy.";
Biochemistry 32:1164-1171(1993).
[37]
STRUCTURE BY NMR OF 279-390.
PubMed=8679613; DOI=10.1021/bi9604946;
Hinck A.P., Archer S.J., Qian S.W., Roberts A.B., Sporn M.B.,
Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J.,
Torchia D.A.;
"Transforming growth factor beta 1: three-dimensional structure in solution
and comparison with the X-ray structure of transforming growth factor beta
2.";
Biochemistry 35:8517-8534(1996).
[38] {ECO:0000244|PDB:3KFD}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 279-390 IN COMPLEX WITH TGFBR1
AND TGFBR2, FUNCTION, SUBUNIT, AND DISULFIDE BONDS.
PubMed=20207738; DOI=10.1074/jbc.m109.079921;
Radaev S., Zou Z., Huang T., Lafer E.M., Hinck A.P., Sun P.D.;
"Ternary complex of transforming growth factor-beta1 reveals isoform-
specific ligand recognition and receptor recruitment in the superfamily.";
J. Biol. Chem. 285:14806-14814(2010).
[39] {ECO:0000244|PDB:4KV5}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 279-390, SUBUNIT, AND DISULFIDE
BONDS.
PubMed=25209176; DOI=10.1002/pro.2548;
Moulin A., Mathieu M., Lawrence C., Bigelow R., Levine M., Hamel C.,
Marquette J.P., Le Parc J., Loux C., Ferrari P., Capdevila C., Dumas J.,
Dumas B., Rak A., Bird J., Qiu H., Pan C.Q., Edmunds T., Wei R.R.;
"Structures of a pan-specific antagonist antibody complexed to different
isoforms of TGFbeta reveal structural plasticity of antibody-antigen
interactions.";
Protein Sci. 23:1698-1707(2014).
[40] {ECO:0000244|PDB:5FFO}
X-RAY CRYSTALLOGRAPHY (3.49 ANGSTROMS) OF 34-390 IN COMPLEX WITH ITGAV AND
ITGB6, FUNCTION, INTERACTION WITH ITGAV AND ITGB6, SUBUNIT, DISULFIDE BOND,
GLYCOSYLATION AT ASN-82, AND MUTAGENESIS OF GLU-75; LEU-158; LEU-160;
PRO-193; 232-LEU--ILE-236; 234-VAL--ILE-236; ASN-237; ASN-254 AND
257-PHE--LEU-260.
PubMed=28117447; DOI=10.1038/nature21035;
Dong X., Zhao B., Iacob R.E., Zhu J., Koksal A.C., Lu C., Engen J.R.,
Springer T.A.;
"Force interacts with macromolecular structure in activation of TGF-beta.";
Nature 542:55-59(2017).
[41] {ECO:0000244|PDB:5VQP}
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 30-390, SUBUNIT, DISULFIDE BONDS,
AND MUTAGENESIS OF ARG-278.
PubMed=29109152; DOI=10.1074/jbc.m117.809657;
Zhao B., Xu S., Dong X., Lu C., Springer T.A.;
"Prodomain-growth factor swapping in the structure of pro-TGF-beta1.";
J. Biol. Chem. 293:1579-1589(2018).
[42]
VARIANT PRO-10.
PubMed=9783545; DOI=10.1359/jbmr.1998.13.10.1569;
Yamada Y., Miyauchi A., Goto J., Takagi Y., Okuizumi H., Kanematsu M.,
Hase M., Takai H., Harada A., Ikeda K.;
"Association of a polymorphism of the transforming growth factor-beta1 gene
with genetic susceptibility to osteoporosis in postmenopausal Japanese
women.";
J. Bone Miner. Res. 13:1569-1576(1998).
[43]
VARIANTS CAEND CYS-218; HIS-218 AND ARG-225.
PubMed=10973241; DOI=10.1038/79128;
Kinoshita A., Saito T., Tomita H., Makita Y., Yoshida K., Ghadami M.,
Yamada K., Kondo S., Ikegawa S., Nishimura G., Fukushima Y., Nakagomi T.,
Saito H., Sugimoto T., Kamegaya M., Hisa K., Murray J.C., Taniguchi N.,
Niikawa N., Yoshiura K.;
"Domain-specific mutations in TGFB1 result in Camurati-Engelmann disease.";
Nat. Genet. 26:19-20(2000).
[44]
VARIANTS CAEND HIS-81; CYS-218 AND ARG-225.
PubMed=11062463; DOI=10.1038/81563;
Janssens K., Gershoni-Baruch R., Guanabens N., Migone N., Ralston S.,
Bonduelle M., Lissens W., Van Maldergem L., Vanhoenacker F., Verbruggen L.,
Van Hul W.;
"Mutations in the gene encoding the latency-associated peptide of TGF-beta
1 cause Camurati-Engelmann disease.";
Nat. Genet. 26:273-275(2000).
[45]
VARIANT PRO-10.
PubMed=12202987; DOI=10.1007/s100380200069;
Watanabe Y., Kinoshita A., Yamada T., Ohta T., Kishino T., Matsumoto N.,
Ishikawa M., Niikawa N., Yoshiura K.;
"A catalog of 106 single-nucleotide polymorphisms (SNPs) and 11 other types
of variations in genes for transforming growth factor-beta1 (TGF-beta1) and
its signaling pathway.";
J. Hum. Genet. 47:478-483(2002).
[46]
CHARACTERIZATION OF VARIANTS CAEND HIS-81; CYS-218; ASP-222 AND ARG-225.
PubMed=12493741; DOI=10.1074/jbc.m208857200;
Janssens K., ten Dijke P., Ralston S.H., Bergmann C., Van Hul W.;
"Transforming growth factor-beta-1 mutations in Camurati-Engelmann disease
lead to increased signaling by altering either activation or secretion of
the mutant protein.";
J. Biol. Chem. 278:7718-7724(2003).
[47]
CHARACTERIZATION OF VARIANT CAEND CYS-218.
PubMed=12843182; DOI=10.1210/jc.2002-020564;
McGowan N.W., MacPherson H., Janssens K., Van Hul W., Frith J.C.,
Fraser W.D., Ralston S.H., Helfrich M.H.;
"A mutation affecting the latency-associated peptide of TGFbeta1 in
Camurati-Engelmann disease enhances osteoclast formation in vitro.";
J. Clin. Endocrinol. Metab. 88:3321-3326(2003).
[48]
VARIANTS CAEND GLY-223 AND ARG-223.
PubMed=15103729; DOI=10.1002/ajmg.a.20671;
Kinoshita A., Fukumaki Y., Shirahama S., Miyahara A., Nishimura G.,
Haga N., Namba A., Ueda H., Hayashi H., Ikegawa S., Seidel J., Niikawa N.,
Yoshiura K.;
"TGFB1 mutations in four new families with Camurati-Engelmann disease:
confirmation of independently arising LAP-domain-specific mutations.";
Am. J. Med. Genet. 127A:104-107(2004).
-!- FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of
the Latency-associated peptide (LAP) and Transforming growth factor
beta-1 (TGF-beta-1) chains, which constitute the regulatory and active
subunit of TGF-beta-1, respectively. {ECO:0000269|PubMed:29109152,
ECO:0000303|PubMed:27252363}.
-!- FUNCTION: [Latency-associated peptide]: Required to maintain the
Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state
during storage in extracellular matrix (PubMed:28117447). Associates
non-covalently with TGF-beta-1 and regulates its activation via
interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP and
LRRC33/NRROS, that control activation of TGF-beta-1 (PubMed:2022183,
PubMed:8617200, PubMed:8939931, PubMed:19750484, PubMed:22278742,
PubMed:19651619). Interaction with LRRC33/NRROS regulates activation of
TGF-beta-1 in macrophages and microglia (Probable). Interaction with
LRRC32/GARP controls activation of TGF-beta-1 on the surface of
activated regulatory T-cells (Tregs) (PubMed:19750484, PubMed:22278742,
PubMed:19651619). Interaction with integrins (ITGAV:ITGB6 or
ITGAV:ITGB8) results in distortion of the Latency-associated peptide
chain and subsequent release of the active TGF-beta-1 (PubMed:22278742,
PubMed:28117447). {ECO:0000269|PubMed:19651619,
ECO:0000269|PubMed:19750484, ECO:0000269|PubMed:2022183,
ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:28117447,
ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931,
ECO:0000305|PubMed:29909984}.
-!- FUNCTION: Transforming growth factor beta-1: Multifunctional protein
that regulates the growth and differentiation of various cell types and
is involved in various processes, such as normal development, immune
function, microglia function and responses to neurodegeneration (By
similarity). Activation into mature form follows different steps:
following cleavage of the proprotein in the Golgi apparatus, Latency-
associated peptide (LAP) and Transforming growth factor beta-1 (TGF-
beta-1) chains remain non-covalently linked rendering TGF-beta-1
inactive during storage in extracellular matrix (PubMed:29109152). At
the same time, LAP chain interacts with 'milieu molecules', such as
LTBP1, LRRC32/GARP and LRRC33/NRROS that control activation of TGF-
beta-1 and maintain it in a latent state during storage in
extracellular milieus (PubMed:2022183, PubMed:8617200, PubMed:8939931,
PubMed:19750484, PubMed:22278742, PubMed:19651619). TGF-beta-1 is
released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin-
binding to LAP stabilizes an alternative conformation of the LAP bowtie
tail and results in distortion of the LAP chain and subsequent release
of the active TGF-beta-1 (PubMed:22278742, PubMed:28117447). Once
activated following release of LAP, TGF-beta-1 acts by binding to TGF-
beta receptors (TGFBR1 and TGFBR2), which transduce signal
(PubMed:20207738). While expressed by many cells types, TGF-beta-1 only
has a very localized range of action within cell environment thanks to
fine regulation of its activation by Latency-associated peptide chain
(LAP) and 'milieu molecules' (By similarity). Plays an important role
in bone remodeling: acts as a potent stimulator of osteoblastic bone
formation, causing chemotaxis, proliferation and differentiation in
committed osteoblasts (By similarity). Can promote either T-helper 17
cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a
concentration-dependent manner (By similarity). At high concentrations,
leads to FOXP3-mediated suppression of RORC and down-regulation of IL-
17 expression, favoring Treg cell development (By similarity). At low
concentrations in concert with IL-6 and IL-21, leads to expression of
the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells
(By similarity). Stimulates sustained production of collagen through
the activation of CREB3L1 by regulated intramembrane proteolysis (RIP)
(PubMed:25310401). Mediates SMAD2/3 activation by inducing its
phosphorylation and subsequent translocation to the nucleus
(PubMed:25893292, PubMed:29483653, PubMed:30696809). Can induce
epithelial-to-mesenchymal transition (EMT) and cell migration in
various cell types (PubMed:25893292, PubMed:30696809).
{ECO:0000250|UniProtKB:P04202, ECO:0000269|PubMed:19651619,
ECO:0000269|PubMed:19750484, ECO:0000269|PubMed:20207738,
ECO:0000269|PubMed:2022183, ECO:0000269|PubMed:22278742,
ECO:0000269|PubMed:25310401, ECO:0000269|PubMed:25893292,
ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152,
ECO:0000269|PubMed:29483653, ECO:0000269|PubMed:30696809,
ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931}.
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:20207738, PubMed:25209176,
PubMed:28117447, PubMed:29109152). Interacts with the serine proteases,
HTRA1 and HTRA3: the interaction with either inhibits TGFB1-mediated
signaling. The HTRA protease activity is required for this inhibition
(By similarity). May interact with THSD4; this interaction may lead to
sequestration by FBN1 microfibril assembly and attenuation of TGFB
signaling (By similarity). Interacts with CD109, DPT and ASPN
(PubMed:9895299, PubMed:16754747, PubMed:17827158). Latency-associated
peptide: Homodimer; disulfide-linked (PubMed:28117447,
PubMed:29109152). Latency-associated peptide: Interacts with
Transforming growth factor beta-1 (TGF-beta-1) chain; interaction is
non-covalent and maintains (TGF-beta-1) in a latent state; each
Latency-associated peptide (LAP) monomer interacts with TGF-beta-1 in
the other monomer (PubMed:29109152). Latency-associated peptide:
Interacts with LTBP1; leading to regulate activation of TGF-beta-1
(PubMed:2022183, PubMed:8617200, PubMed:8939931). Latency-associated
peptide: Interacts with LRRC32/GARP; leading to regulate activation of
TGF-beta-1 on the surface of activated regulatory T-cells (Tregs)
(PubMed:19750484, PubMed:22278742, PubMed:19651619). Interacts with
LRRC33/NRROS; leading to regulate activation of TGF-beta-1 in
macrophages and microglia (Probable). Latency-associated peptide:
Interacts (via cell attachment site) with integrins ITGAV and ITGB6
(ITGAV:ITGB6), leading to release of the active TGF-beta-1
(PubMed:22278742, PubMed:28117447). Latency-associated peptide:
Interacts with NREP; the interaction results in a decrease in TGFB1
autoinduction (By similarity). Latency-associated peptide: Interacts
with HSP90AB1; inhibits latent TGFB1 activation (PubMed:20599762).
Transforming growth factor beta-1: Homodimer; disulfide-linked
(PubMed:20207738, PubMed:25209176, PubMed:28117447, PubMed:29109152).
Transforming growth factor beta-1: Interacts with TGF-beta receptors
(TGFBR1 and TGFBR2), leading to signal transduction (PubMed:20207738).
{ECO:0000250|UniProtKB:P04202, ECO:0000269|PubMed:16754747,
ECO:0000269|PubMed:17827158, ECO:0000269|PubMed:19651619,
ECO:0000269|PubMed:19750484, ECO:0000269|PubMed:20207738,
ECO:0000269|PubMed:2022183, ECO:0000269|PubMed:20599762,
ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:25209176,
ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152,
ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931,
ECO:0000269|PubMed:9895299, ECO:0000305|PubMed:29909984}.
-!- INTERACTION:
P01137; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-779636, EBI-10173507;
P01137; P05067: APP; NbExp=3; IntAct=EBI-779636, EBI-77613;
P01137; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-779636, EBI-744545;
P01137; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-779636, EBI-3867333;
P01137; Q14689: DIP2A; NbExp=2; IntAct=EBI-779636, EBI-2564275;
P01137; P17813: ENG; NbExp=2; IntAct=EBI-779636, EBI-2834630;
P01137; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-779636, EBI-11977403;
P01137; Q12841: FSTL1; NbExp=2; IntAct=EBI-779636, EBI-2349801;
P01137; P49639: HOXA1; NbExp=3; IntAct=EBI-779636, EBI-740785;
P01137; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-779636, EBI-11959885;
P01137; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-779636, EBI-10171774;
P01137; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-779636, EBI-10302392;
P01137; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-779636, EBI-11962058;
P01137; Q5T751: LCE1C; NbExp=3; IntAct=EBI-779636, EBI-12224199;
P01137; Q5T752: LCE1D; NbExp=3; IntAct=EBI-779636, EBI-11741311;
P01137; O14633: LCE2B; NbExp=3; IntAct=EBI-779636, EBI-11478468;
P01137; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-779636, EBI-11973993;
P01137; Q5TA76: LCE3A; NbExp=3; IntAct=EBI-779636, EBI-9394625;
P01137; Q5TA77: LCE3B; NbExp=3; IntAct=EBI-779636, EBI-11974495;
P01137; Q9BYE3: LCE3D; NbExp=3; IntAct=EBI-779636, EBI-6658837;
P01137; O60711: LPXN; NbExp=3; IntAct=EBI-779636, EBI-744222;
P01137; Q14392: LRRC32; NbExp=2; IntAct=EBI-779636, EBI-15796956;
P01137; Q14766-1: LTBP1; NbExp=4; IntAct=EBI-779636, EBI-11173861;
P01137; P50222: MEOX2; NbExp=3; IntAct=EBI-779636, EBI-748397;
P01137; P07237: P4HB; NbExp=3; IntAct=EBI-779636, EBI-395883;
P01137; Q12837: POU4F2; NbExp=3; IntAct=EBI-779636, EBI-17236143;
P01137; P11464: PSG1; NbExp=3; IntAct=EBI-779636, EBI-716740;
P01137; P01137: TGFB1; NbExp=2; IntAct=EBI-779636, EBI-779636;
P01137; P36897: TGFBR1; NbExp=2; IntAct=EBI-779636, EBI-1027557;
P01137; P37173: TGFBR2; NbExp=6; IntAct=EBI-779636, EBI-296151;
P01137; Q03167: TGFBR3; NbExp=2; IntAct=EBI-779636, EBI-2852679;
P01137; P07996: THBS1; NbExp=2; IntAct=EBI-779636, EBI-2530274;
P01137; Q90998: TGFBR3; Xeno; NbExp=2; IntAct=EBI-779636, EBI-6620843;
PRO_0000033762; P11464: PSG1; NbExp=2; IntAct=EBI-15487336, EBI-716740;
-!- SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted,
extracellular space, extracellular matrix
{ECO:0000269|PubMed:17827158}.
-!- SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted
{ECO:0000269|PubMed:17827158, ECO:0000269|PubMed:29483653}.
-!- TISSUE SPECIFICITY: Highly expressed in bone (PubMed:11746498,
PubMed:17827158). Abundantly expressed in articular cartilage and
chondrocytes and is increased in osteoarthritis (OA) (PubMed:11746498,
PubMed:17827158). Colocalizes with ASPN in chondrocytes within OA
lesions of articular cartilage (PubMed:17827158).
{ECO:0000269|PubMed:11746498, ECO:0000269|PubMed:17827158}.
-!- DOMAIN: [Latency-associated peptide]: The 'straitjacket' and 'arm'
domains encircle the Transforming growth factor beta-1 (TGF-beta-1)
monomers and are fastened together by strong bonding between Lys-56 and
Tyr-103/Tyr-104. {ECO:0000250|UniProtKB:P07200}.
-!- DOMAIN: [Latency-associated peptide]: The cell attachment site motif
mediates binding to integrins (ITGAV:ITGB6 or ITGAV:ITGB8)
(PubMed:28117447). The motif locates to a long loop in the arm domain
called the bowtie tail (PubMed:28117447). Integrin-binding stabilizes
an alternative conformation of the bowtie tail (PubMed:28117447).
Activation by integrin requires force application by the actin
cytoskeleton, which is resisted by the 'milieu molecules' (such as
LTBP1, LRRC32/GARP and/or LRRC33/NRROS), resulting in distortion of the
prodomain and release of the active TGF-beta-1 (PubMed:28117447).
{ECO:0000269|PubMed:28117447}.
-!- PTM: Transforming growth factor beta-1 proprotein: The precursor
proprotein is cleaved in the Golgi apparatus by FURIN to form
Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated
peptide (LAP) chains, which remain non-covalently linked, rendering
TGF-beta-1 inactive. {ECO:0000269|PubMed:7737999}.
-!- PTM: [Latency-associated peptide]: N-glycosylated (PubMed:3162913,
PubMed:2493139, PubMed:28117447). Deglycosylation leads to activation
of Transforming growth factor beta-1 (TGF-beta-1); mechanisms
triggering deglycosylation-driven activation of TGF-beta-1 are however
unclear (PubMed:2493139). {ECO:0000269|PubMed:2493139,
ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:3162913}.
-!- POLYMORPHISM: In post-menopausal Japanese women, the frequency of Leu-
10 is higher in subjects with osteoporosis than in controls.
{ECO:0000269|PubMed:9783545}.
-!- DISEASE: Camurati-Engelmann disease (CAEND) [MIM:131300]: An autosomal
dominant disorder characterized by hyperostosis and sclerosis of the
diaphyses of long bones. The disease typically presents in early
childhood with pain, muscular weakness and waddling gait, and in some
cases other features such as exophthalmos, facial paralysis, hearing
difficulties and loss of vision. {ECO:0000269|PubMed:10973241,
ECO:0000269|PubMed:11062463, ECO:0000269|PubMed:12493741,
ECO:0000269|PubMed:12843182, ECO:0000269|PubMed:15103729}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Inflammatory bowel disease, immunodeficiency, and
encephalopathy (IBDIMDE) [MIM:618213]: An autosomal recessive disorder
characterized by severe infantile inflammatory bowel disease
manifesting as bloody diarrhea and failure to thrive, global
developmental delay, epilepsy, brain atrophy and encephalopathy.
Affected individuals suffer from recurrent infections associated with
impaired T-cell response to stimulation and decreased T-cell subsets,
including regulatory and helper T cells. {ECO:0000269|PubMed:29483653}.
Note=The disease is caused by mutations affecting the gene represented
in this entry.
-!- MISCELLANEOUS: TGF-beta-1 is inactivated by fresolimumab (also named
GC1008), a monoclonal-neutralizing antibody.
{ECO:0000269|PubMed:25209176}.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=TGF beta-1 entry;
URL="https://en.wikipedia.org/wiki/TGF_beta_1";
---------------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; X05839; CAA29283.1; -; Genomic_DNA.
EMBL; X05840; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X05843; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X05844; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X05849; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X05850; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X02812; CAA26580.1; -; mRNA.
EMBL; BT007245; AAP35909.1; -; mRNA.
EMBL; AK291907; BAF84596.1; -; mRNA.
EMBL; CH471126; EAW57032.1; -; Genomic_DNA.
EMBL; BC001180; AAH01180.1; -; mRNA.
EMBL; BC000125; AAH00125.1; -; mRNA.
EMBL; BC022242; AAH22242.1; -; mRNA.
EMBL; M38449; AAA36735.1; -; mRNA.
CCDS; CCDS33031.1; -.
PIR; A27513; WFHU2.
RefSeq; NP_000651.3; NM_000660.6.
PDB; 1KLA; NMR; -; A/B=279-390.
PDB; 1KLC; NMR; -; A/B=279-390.
PDB; 1KLD; NMR; -; A/B=279-390.
PDB; 3KFD; X-ray; 3.00 A; A/B/C/D=279-390.
PDB; 4KV5; X-ray; 3.00 A; A/B/C/D=279-390.
PDB; 5FFO; X-ray; 3.49 A; C/D/G/H=34-390.
PDB; 5VQP; X-ray; 2.90 A; A=30-390.
PDB; 6P7J; X-ray; 3.50 A; A=30-278.
PDBsum; 1KLA; -.
PDBsum; 1KLC; -.
PDBsum; 1KLD; -.
PDBsum; 3KFD; -.
PDBsum; 4KV5; -.
PDBsum; 5FFO; -.
PDBsum; 5VQP; -.
PDBsum; 6P7J; -.
SMR; P01137; -.
BioGRID; 112898; 226.
ComplexPortal; CPX-529; TGF-beta-1-TGFR complex.
ComplexPortal; CPX-602; TGF-beta-1 complex.
CORUM; P01137; -.
DIP; DIP-5934N; -.
IntAct; P01137; 94.
MINT; P01137; -.
STRING; 9606.ENSP00000221930; -.
BindingDB; P01137; -.
ChEMBL; CHEMBL1795178; -.
DrugBank; DB10770; Foreskin fibroblast (neonatal).
DrugBank; DB10772; Foreskin keratinocyte (neonatal).
DrugBank; DB00070; Hyaluronidase (ovine).
DrugBank; DB01162; Terazosin.
DrugBank; DB06205; Vorhyaluronidase alfa.
GlyConnect; 1835; -.
iPTMnet; P01137; -.
PhosphoSitePlus; P01137; -.
BioMuta; TGFB1; -.
DMDM; 135674; -.
OGP; P01137; -.
EPD; P01137; -.
jPOST; P01137; -.
MassIVE; P01137; -.
MaxQB; P01137; -.
PaxDb; P01137; -.
PeptideAtlas; P01137; -.
PRIDE; P01137; -.
ProteomicsDB; 51337; -.
ABCD; P01137; 5 sequenced antibodies.
DNASU; 7040; -.
GeneID; 7040; -.
KEGG; hsa:7040; -.
UCSC; uc002oqh.4; human.
CTD; 7040; -.
DisGeNET; 7040; -.
EuPathDB; HostDB:ENSG00000105329.9; -.
GeneCards; TGFB1; -.
GeneReviews; TGFB1; -.
HGNC; HGNC:11766; TGFB1.
HPA; ENSG00000105329; Low tissue specificity.
MalaCards; TGFB1; -.
MIM; 131300; phenotype.
MIM; 190180; gene.
MIM; 618213; phenotype.
neXtProt; NX_P01137; -.
Orphanet; 1328; Camurati-Engelmann disease.
Orphanet; 586; Cystic fibrosis.
Orphanet; 565788; Infantile inflammatory bowel disease with neurological involvement.
PharmGKB; PA350; -.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
HOGENOM; CLU_039840_0_0_1; -.
InParanoid; P01137; -.
KO; K13375; -.
OrthoDB; 853728at2759; -.
PhylomeDB; P01137; -.
TreeFam; TF318514; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-168277; Influenza Virus Induced Apoptosis.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-3304356; SMAD2/3 Phosphorylation Motif Mutants in Cancer.
Reactome; R-HSA-3642279; TGFBR2 MSI Frameshift Mutants in Cancer.
Reactome; R-HSA-3645790; TGFBR2 Kinase Domain Mutants in Cancer.
Reactome; R-HSA-3656532; TGFBR1 KD Mutants in Cancer.
Reactome; R-HSA-3656535; TGFBR1 LBD Mutants in Cancer.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-8941855; RUNX3 regulates CDKN1A transcription.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
SignaLink; P01137; -.
SIGNOR; P01137; -.
BioGRID-ORCS; 7040; 2 hits in 791 CRISPR screens.
ChiTaRS; TGFB1; human.
EvolutionaryTrace; P01137; -.
GeneWiki; TGF_beta_1; -.
GenomeRNAi; 7040; -.
Pharos; P01137; Tchem.
PRO; PR:P01137; -.
Proteomes; UP000005640; Unplaced.
RNAct; P01137; protein.
Bgee; ENSG00000105329; Expressed in leukocyte and 169 other tissues.
Genevisible; P01137; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0009986; C:cell surface; IMP:BHF-UCL.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0003823; F:antigen binding; IPI:UniProtKB.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IMP:AgBase.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IDA:BHF-UCL.
GO; GO:0034714; F:type III transforming growth factor beta receptor binding; IMP:AgBase.
GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
GO; GO:0006754; P:ATP biosynthetic process; IDA:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0045216; P:cell-cell junction organization; IDA:BHF-UCL.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL.
GO; GO:0002062; P:chondrocyte differentiation; IDA:UniProtKB.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IDA:UniProtKB.
GO; GO:0002248; P:connective tissue replacement involved in inflammatory response wound healing; TAS:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:1990402; P:embryonic liver development; ISS:BHF-UCL.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:UniProtKB.
GO; GO:0085029; P:extracellular matrix assembly; IDA:BHF-UCL.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0007507; P:heart development; ISS:BHF-UCL.
GO; GO:0003179; P:heart valve morphogenesis; ISS:BHF-UCL.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IDA:UniProtKB.
GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0048535; P:lymph node development; ISS:UniProtKB.
GO; GO:0010742; P:macrophage derived foam cell differentiation; IC:BHF-UCL.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IDA:UniProtKB.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IDA:BHF-UCL.
GO; GO:0070168; P:negative regulation of biomineral tissue development; IDA:BHF-UCL.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:HGNC-UCL.
GO; GO:0045596; P:negative regulation of cell differentiation; IEP:CACAO.
GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0045918; P:negative regulation of cytolysis; IDA:ARUK-UCL.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:BHF-UCL.
GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; IC:BHF-UCL.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
GO; GO:0060965; P:negative regulation of gene silencing by miRNA; IGI:BHF-UCL.
GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; IDA:UniProtKB.
GO; GO:0010936; P:negative regulation of macrophage cytokine production; IDA:DFLAT.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:BHF-UCL.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IDA:UniProtKB.
GO; GO:1902894; P:negative regulation of pri-miRNA transcription by RNA polymerase II; NAS:BHF-UCL.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IGI:BHF-UCL.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0001843; P:neural tube closure; ISS:BHF-UCL.
GO; GO:0021915; P:neural tube development; ISS:BHF-UCL.
GO; GO:0043932; P:ossification involved in bone remodeling; IEP:BHF-UCL.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:UniProtKB.
GO; GO:0006796; P:phosphate-containing compound metabolic process; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0030501; P:positive regulation of bone mineralization; IEP:BHF-UCL.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:CACAO.
GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; IDA:BHF-UCL.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IDA:BHF-UCL.
GO; GO:0050921; P:positive regulation of chemotaxis; IDA:BHF-UCL.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:1901203; P:positive regulation of extracellular matrix assembly; IC:BHF-UCL.
GO; GO:0010763; P:positive regulation of fibroblast migration; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; IDA:MGI.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
GO; GO:0014008; P:positive regulation of microglia differentiation; ISS:UniProtKB.
GO; GO:1901666; P:positive regulation of NAD+ ADP-ribosyltransferase activity; IDA:BHF-UCL.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:BHF-UCL.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:BHF-UCL.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0050714; P:positive regulation of protein secretion; IDA:BHF-UCL.
GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:BHF-UCL.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:BHF-UCL.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; TAS:BHF-UCL.
GO; GO:0043117; P:positive regulation of vascular permeability; IDA:UniProtKB.
GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0032801; P:receptor catabolic process; IDA:BHF-UCL.
GO; GO:0051098; P:regulation of binding; ISS:UniProtKB.
GO; GO:0060312; P:regulation of blood vessel remodeling; NAS:BHF-UCL.
GO; GO:0030334; P:regulation of cell migration; TAS:BHF-UCL.
GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
GO; GO:0051101; P:regulation of DNA binding; ISS:UniProtKB.
GO; GO:0042306; P:regulation of protein import into nucleus; ISS:UniProtKB.
GO; GO:0060390; P:regulation of SMAD protein signal transduction; IDA:UniProtKB.
GO; GO:0016202; P:regulation of striated muscle tissue development; ISS:UniProtKB.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0070723; P:response to cholesterol; IDA:BHF-UCL.
GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL.
GO; GO:0032570; P:response to progesterone; IDA:BHF-UCL.
GO; GO:0009611; P:response to wounding; IEP:BHF-UCL.
GO; GO:0007435; P:salivary gland morphogenesis; IEP:BHF-UCL.
GO; GO:0007183; P:SMAD protein complex assembly; IDA:BHF-UCL.
GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:1905313; P:transforming growth factor beta receptor signaling pathway involved in heart development; ISS:BHF-UCL.
GO; GO:0001570; P:vasculogenesis; ISS:BHF-UCL.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
DisProt; DP01252; -.
Gene3D; 2.10.90.10; -; 1.
IDEAL; IID00534; -.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR016319; TGF-beta.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR003939; TGFb1.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
PIRSF; PIRSF001787; TGF-beta; 1.
PRINTS; PR01423; TGFBETA.
PRINTS; PR01424; TGFBETA1.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues;
Direct protein sequencing; Disease mutation; Disulfide bond;
Extracellular matrix; Glycoprotein; Growth factor; Mitogen; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1..29
/evidence="ECO:0000269|PubMed:3162913"
CHAIN 30..278
/note="Latency-associated peptide"
/evidence="ECO:0000305|PubMed:2982829,
ECO:0000305|PubMed:3162913, ECO:0000305|PubMed:7737999,
ECO:0000305|PubMed:8471846"
/id="PRO_0000033762"
CHAIN 279..390
/note="Transforming growth factor beta-1"
/evidence="ECO:0000305|PubMed:2982829,
ECO:0000305|PubMed:3162913, ECO:0000305|PubMed:7737999,
ECO:0000305|PubMed:8471846"
/id="PRO_0000033763"
REGION 30..74
/note="Straightjacket domain"
/evidence="ECO:0000250|UniProtKB:P07200"
REGION 75..271
/note="Arm domain"
/evidence="ECO:0000250|UniProtKB:P07200"
REGION 226..252
/note="Bowtie tail"
/evidence="ECO:0000269|PubMed:28117447"
MOTIF 244..246
/note="Cell attachment site"
/evidence="ECO:0000269|PubMed:28117447"
SITE 278..279
/note="Cleavage; by FURIN"
/evidence="ECO:0000269|PubMed:7737999"
CARBOHYD 82
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:5FFO,
ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:28117447"
CARBOHYD 136
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 176
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 33
/note="Interchain (with C-1359 or C-1384 in LTBP1); in
inactive form"
/evidence="ECO:0000305|PubMed:22278742"
DISULFID 223
/note="Interchain (with C-225)"
/evidence="ECO:0000244|PDB:5FFO, ECO:0000244|PDB:5VQP,
ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152"
DISULFID 225
/note="Interchain (with C-223)"
/evidence="ECO:0000244|PDB:5FFO, ECO:0000244|PDB:5VQP,
ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152"
DISULFID 285..294
/evidence="ECO:0000244|PDB:3KFD, ECO:0000244|PDB:4KV5,
ECO:0000244|PDB:5FFO, ECO:0000244|PDB:5VQP,
ECO:0000269|PubMed:20207738, ECO:0000269|PubMed:25209176,
ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152"
DISULFID 293..356
/evidence="ECO:0000244|PDB:3KFD, ECO:0000244|PDB:4KV5,
ECO:0000244|PDB:5FFO, ECO:0000244|PDB:5VQP,
ECO:0000269|PubMed:20207738, ECO:0000269|PubMed:25209176,
ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152"
DISULFID 322..387
/evidence="ECO:0000244|PDB:3KFD, ECO:0000244|PDB:4KV5,
ECO:0000244|PDB:5FFO, ECO:0000244|PDB:5VQP,
ECO:0000269|PubMed:20207738, ECO:0000269|PubMed:25209176,
ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152"
DISULFID 326..389
/evidence="ECO:0000244|PDB:3KFD, ECO:0000244|PDB:4KV5,
ECO:0000244|PDB:5FFO, ECO:0000244|PDB:5VQP,
ECO:0000269|PubMed:20207738, ECO:0000269|PubMed:25209176,
ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152"
DISULFID 355
/note="Interchain"
/evidence="ECO:0000244|PDB:3KFD, ECO:0000244|PDB:4KV5,
ECO:0000244|PDB:5FFO, ECO:0000269|PubMed:20207738,
ECO:0000269|PubMed:25209176, ECO:0000269|PubMed:28117447"
VARIANT 10
/note="L -> P (associated with higher bone mineral density
and lower frequency of vertebral fractures in Japanese
post-menopausal women; dbSNP:rs1800470)"
/evidence="ECO:0000269|PubMed:12202987,
ECO:0000269|PubMed:3861940, ECO:0000269|PubMed:9783545"
/id="VAR_016171"
VARIANT 25
/note="R -> P (in dbSNP:rs1800471)"
/evidence="ECO:0000269|PubMed:3861940"
/id="VAR_016172"
VARIANT 45
/note="R -> C (in IBDIMDE; decreased TGFB1-mediated
activation of SMAD signaling; reduced levels of secreated
TGFB1)"
/evidence="ECO:0000269|PubMed:29483653"
/id="VAR_081584"
VARIANT 81
/note="Y -> H (in CAEND; leads to TGF-beta-1 intracellular
accumulation)"
/evidence="ECO:0000269|PubMed:11062463,
ECO:0000269|PubMed:12493741"
/id="VAR_017607"
VARIANT 110
/note="R -> C (in IBDIMDE; decreased TGFB1-mediated
activation of SMAD signaling; reduced levels of secreated
TGFB1)"
/evidence="ECO:0000269|PubMed:29483653"
/id="VAR_081585"
VARIANT 218
/note="R -> C (in CAEND; higher levels of active TGF-beta-1
in the culture medium; enhances osteoclast formation in
vitro)"
/evidence="ECO:0000269|PubMed:10973241,
ECO:0000269|PubMed:11062463, ECO:0000269|PubMed:12493741,
ECO:0000269|PubMed:12843182"
/id="VAR_017608"
VARIANT 218
/note="R -> H (in CAEND)"
/evidence="ECO:0000269|PubMed:10973241"
/id="VAR_017609"
VARIANT 222
/note="H -> D (in CAEND; sporadic case; higher levels of
active TGF-beta-1 in the culture medium)"
/evidence="ECO:0000269|PubMed:12493741"
/id="VAR_017610"
VARIANT 223
/note="C -> G (in CAEND)"
/evidence="ECO:0000269|PubMed:15103729"
/id="VAR_067303"
VARIANT 223
/note="C -> R (in CAEND)"
/evidence="ECO:0000269|PubMed:15103729"
/id="VAR_067304"
VARIANT 225
/note="C -> R (in CAEND; higher levels of active TGF-beta-1
in the culture medium)"
/evidence="ECO:0000269|PubMed:10973241,
ECO:0000269|PubMed:11062463, ECO:0000269|PubMed:12493741"
/id="VAR_017611"
VARIANT 263
/note="T -> I (in dbSNP:rs1800472)"
/id="VAR_016173"
VARIANT 387
/note="C -> R (in IBDIMDE; loss of TGFB1-mediated
activation of SMAD signaling; mutant TGFB1 is not
secreted)"
/evidence="ECO:0000269|PubMed:29483653"
/id="VAR_081586"
MUTAGEN 33
/note="C->S: Abolishes interchain disulfide bond with LTBP1
and/or LRRC32, and subsequent regulation of activation of
TGF-beta-1."
/evidence="ECO:0000269|PubMed:22278742,
ECO:0000269|PubMed:8617200"
MUTAGEN 75
/note="E->A: Does not affect integrin-binding or activation
of TGF-beta-1."
/evidence="ECO:0000269|PubMed:28117447"
MUTAGEN 158
/note="L->A: Does not affect integrin-binding or activation
of TGF-beta-1."
/evidence="ECO:0000269|PubMed:28117447"
MUTAGEN 160
/note="L->A,R: Does not affect integrin-binding or
activation of TGF-beta-1."
/evidence="ECO:0000269|PubMed:28117447"
MUTAGEN 193
/note="P->A,R: Does not affect integrin-binding or
activation of TGF-beta-1."
/evidence="ECO:0000269|PubMed:28117447"
MUTAGEN 232..236
/note="LQVDI->GQGDG: Strongly inhibits integrin-binding and
activation of TGF-beta-1."
/evidence="ECO:0000269|PubMed:28117447"
MUTAGEN 234..236
/note="VDI->GDG: Strongly inhibits integrin-binding and
activation of TGF-beta-1."
/evidence="ECO:0000269|PubMed:28117447"
MUTAGEN 237
/note="N->A: Does not affect integrin-binding or activation
of TGF-beta-1."
/evidence="ECO:0000269|PubMed:28117447"
MUTAGEN 254
/note="N->A: Does not affect integrin-binding or activation
of TGF-beta-1."
/evidence="ECO:0000269|PubMed:28117447"
MUTAGEN 257..260
/note="FLLL->GLLG: Strongly inhibits integrin-binding and
activation of TGF-beta-1."
/evidence="ECO:0000269|PubMed:28117447"
MUTAGEN 278
/note="R->A: Prevents cleavage and subsequent maturation of
the protein. Generated in order to mimic the structure of
the Transforming growth factor beta-1 proprotein."
/evidence="ECO:0000269|PubMed:29109152"
CONFLICT 159
/note="R -> RR (in Ref. 2; CAA26580)"
/evidence="ECO:0000305"
HELIX 33..57
/evidence="ECO:0000244|PDB:5VQP"
STRAND 70..72
/evidence="ECO:0000244|PDB:5FFO"
HELIX 75..85
/evidence="ECO:0000244|PDB:5VQP"
STRAND 107..112
/evidence="ECO:0000244|PDB:5VQP"
TURN 123..126
/evidence="ECO:0000244|PDB:5VQP"
STRAND 130..136
/evidence="ECO:0000244|PDB:5VQP"
HELIX 137..143
/evidence="ECO:0000244|PDB:5VQP"
STRAND 144..146
/evidence="ECO:0000244|PDB:5FFO"
HELIX 147..149
/evidence="ECO:0000244|PDB:5VQP"
STRAND 150..159
/evidence="ECO:0000244|PDB:5VQP"
STRAND 166..174
/evidence="ECO:0000244|PDB:5VQP"
TURN 175..177
/evidence="ECO:0000244|PDB:5VQP"
STRAND 178..187
/evidence="ECO:0000244|PDB:5VQP"
STRAND 194..199
/evidence="ECO:0000244|PDB:5VQP"
HELIX 201..209
/evidence="ECO:0000244|PDB:5VQP"
STRAND 213..228
/evidence="ECO:0000244|PDB:5VQP"
STRAND 231..238
/evidence="ECO:0000244|PDB:5VQP"
STRAND 242..244
/evidence="ECO:0000244|PDB:5FFO"
TURN 245..247
/evidence="ECO:0000244|PDB:5VQP"
STRAND 251..254
/evidence="ECO:0000244|PDB:5VQP"
STRAND 257..262
/evidence="ECO:0000244|PDB:5VQP"
HELIX 265..268
/evidence="ECO:0000244|PDB:5VQP"
TURN 282..284
/evidence="ECO:0000244|PDB:1KLC"
HELIX 285..288
/evidence="ECO:0000244|PDB:5VQP"
STRAND 290..301
/evidence="ECO:0000244|PDB:5VQP"
TURN 302..305
/evidence="ECO:0000244|PDB:5VQP"
STRAND 311..313
/evidence="ECO:0000244|PDB:5VQP"
STRAND 315..323
/evidence="ECO:0000244|PDB:5VQP"
STRAND 330..332
/evidence="ECO:0000244|PDB:3KFD"
HELIX 335..346
/evidence="ECO:0000244|PDB:3KFD"
STRAND 347..349
/evidence="ECO:0000244|PDB:3KFD"
STRAND 350..353
/evidence="ECO:0000244|PDB:5FFO"
STRAND 355..370
/evidence="ECO:0000244|PDB:5VQP"
STRAND 373..390
/evidence="ECO:0000244|PDB:5VQP"
SEQUENCE 390 AA; 44341 MW; 75391614250288FE CRC64;
MPPSGLRLLL LLLPLLWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA
SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESAEPEPEPE ADYYAKEVTR VLMVETHNEI
YDKFKQSTHS IYMFFNTSEL REAVPEPVLL SRAELRLLRL KLKVEQHVEL YQKYSNNSWR
YLSNRLLAPS DSPEWLSFDV TGVVRQWLSR GGEIEGFRLS AHCSCDSRDN TLQVDINGFT
TGRRGDLATI HGMNRPFLLL MATPLERAQH LQSSRHRRAL DTNYCFSSTE KNCCVRQLYI
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPCCVPQA
LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS


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RF004-2.5 rHuman TGF beta-3 Active; Transforming growth factor beta-3; TGF-beta-3 2.5ug
RF004-5 rHuman TGF beta-3 Active; Transforming growth factor beta-3; TGF-beta-3 5ug
RF003-2.5 rHuman TGF beta-2 Active; Transforming growth factor beta-2; TGF-beta-2 2.5ug
AS10 1397 Antibody: TGF-beta | transforming growth factor beta , Host: chicken, polyclonal, Comfirmed reactivity: human, mouse, rat, swine TGF (beta) 100
32-224 TGF beta(transforming growth factor beta), with 390-amino acid protein (about 43 kDa), is a multifunctional peptide that controls proliferation, differentiation, and other functions in many cell types 0.1 mL
Pathways :
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1370: TGF Beta Signaling Pathway
WP505: TGF Beta Signaling Pathway
WP1897: Regulation of beta-cell development
WP368: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP871: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1224: EBV LMP1 signaling
WP401: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1048: TGF Beta Signaling Pathway
WP1434: Osteopontin Signaling
WP542: Electron Transport Chain
WP1061: Fatty Acid Beta Oxidation
WP1571: EBV LMP1 signaling
WP25: Fatty Acid Beta Oxidation 3

Related Genes :
[TGFB1 TGFB] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB2] Transforming growth factor beta-2 proprotein (Cetermin) (Glioblastoma-derived T-cell suppressor factor) (G-TSF) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[TGFB3] Transforming growth factor beta-3 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-3 (TGF-beta-3)]
[TGFB2] Transforming growth factor beta-2 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFBR1 ALK5 SKR4] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Activin A receptor type II-like protein kinase of 53kD) (Activin receptor-like kinase 5) (ALK-5) (ALK5) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr3] Transforming growth factor beta receptor type 3 (TGF-beta receptor type 3) (TGFR-3) (Betaglycan) (Transforming growth factor beta receptor III) (TGF-beta receptor type III)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (ESK2) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[MAP3K7 TAK1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[Lefty1 Ebaf Lefty Stra3 Tgfb4] Left-right determination factor 1 (Protein lefty-1) (Lefty protein) (Stimulated by retinoic acid gene 3 protein) (Transforming growth factor beta-4) (TGF-beta-4)
[TGFBR2] TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TbetaR-II)
[Map3k7 Tak1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[LEFTY2 EBAF LEFTA LEFTYA TGFB4 PSEC0024] Left-right determination factor 2 (Endometrial bleeding-associated factor) (Left-right determination factor A) (Protein lefty-2) (Protein lefty-A) (Transforming growth factor beta-4) (TGF-beta-4)
[Nrros Lrrc33] Transforming growth factor beta activator LRRC33 (Leucine-rich repeat-containing protein 33) (Negative regulator of reactive oxygen species)
[LTBP4] Latent-transforming growth factor beta-binding protein 4 (LTBP-4)
[tgfb1] Transforming growth factor beta-1 proprotein (TGF-beta-5) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]

Bibliography :
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